Structural insights into membrane interaction and caveolar targeting of 
dynamin-like EHD2

Shah, C.; Hegde, B. G.; Morén, B.; Behrmann, E.; Mielke, T.; Moenke, G.; Spahn, C. M. T.; Lundmark, R.; Daumke, O.; Langen, R.

doi:10.1016/j.str.2013.12.015

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Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2

Shah, C., Hegde, B. G., Morén, B., Behrmann, E., Mielke, T., Moenke, G., et al. (2014). Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2. Structure, 22(3), 409-20. doi:10.1016/j.str.2013.12.015.

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Shah, C., Author
Hegde, B. G., Author
Morén, B., Author
Behrmann, E.¹, Author
Mielke, T., Author
Moenke, G., Author
Spahn, C. M. T., Author
Lundmark, R., Author
Daumke, O., Author
Langen, R., Author

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Abstract: The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a hydrophobic pocket of the GTPase domain in solution and can be released into the membrane. Cryoelectron microscopy demonstrated that the N terminus is not essential for oligomerization of EHD2 into a membrane-anchored scaffold. Instead, we found a function of the N terminus in regulating targeting and stable association of EHD2 to caveolae. Our data uncover an unexpected, membrane-induced regulatory switch in EHD2 and demonstrate the versatility of EPR to study structure and function of dynamin superfamily proteins.

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Dates: Date issued: 2014

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Identifiers: Other: 24508342
DOI: 10.1016/j.str.2013.12.015
ISSN: 1878-4186 (Electronic)
ISSN: 0969-2126 (Linking)

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Title: Structure

Alternative Title : Structure

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Pages: - Volume / Issue: 22 (3) Sequence Number: - Start / End Page: 409 - 20 Identifier: -